The Purification and Concentration of Diphtheria Toxin

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The Purification and Concentration of Diphtheria Toxin: III. Separation of Toxin from Bacterial Protein.

Diphtheria toxin purified by a variety of methods has always contained bacterial protein. This raises the question whether the predominant protein in purified preparations is a fragment of the bacterial protoplasm which carries the toxin, or is itself the toxin. In a previous paper (Eaton, 1936b) it was shown that in various purified preparations there is no relation between the titer of bacter...

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The Purification and Concentration of Diphtheria Toxoid

By precipitation with acetone at 4 degrees C. a refined diphtheria toxoid was obtained as a dry powder, readily soluble in aqueous solutions. The powder itself appears to be stable. When dissolved in half the original volume of physiological salt solution, the toxoid remained stable, in the cold room, for a period of 7 months. Only toxoids should be used which have been completely detoxified by...

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production and purification of polyclonal antibodies against diphtheria toxin

diphtheria is a fatal disease caused by exotoxin of corynebacterium     diphtheria .  this toxin consists of   two chains, catalytic chain (a) and binding (b) chain. by binding chain (b),   the toxin binds to its receptor on numerous body cells such as myocardial,   kidney and peripheral nerve cells. after entering, catalytic chain (a)   inhibits protein synthesis and finally can cause cell dea...

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Purification of diphtheria toxin receptor from Vero cells.

Diphtheria toxin receptor has been solubilized from Vero cell membranes with octyl beta-D-glucoside. CRM197, the product of a mutated diphtheria toxin gene, was used for the identification of the receptor. The binding activity of the solubilized receptor was assayed by precipitating the receptor with acetone in the presence of phospholipids and carrier proteins. The solubilized receptor was pur...

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ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 1937

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.34.2.139-151.1937